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Oligomerization activated apoptosis and its regulation

등록일
2005년 2월 17일 15시 59분 15초
접수번호
1001
발표코드
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발표시간
금 14시 : 30분
발표형식
심포지엄
발표분야
생명화학 - 생명Ⅰ: 신호전달과 분자 스위치
저자 및
공동저자
이영태, 홍종희, A. Roy, 고윤미, 김태형, H.M.T. Nguyen, 이진희, 김기선
한국과학기술연구원 의과학센터,
The death inducing signaling complex (DISC) is required for the activation of procaspase-8 but the molecular mechanism of this early event is not yet clear. Based on the structural features of partial DISC composed of death domains of Fas and FADD, we propose a new model for procaspase-8 activation. Each death domain stays as a monomer in solution but they form a distinctive heterooligomer when two domains are mixed. This suggests that FADD has to be incorporated into high-order complex for effective procaspase-8 activation. The facts that the Fas death domain increased the affinity of procaspase-8 for FADD suggest that Fas-FADD oligomerization contributed to the facilitation of caspase-8 activation. We propose that FADD is not just a passive component recruited to the engaged receptor but plays an active role in receptor clustering, and apoptosis can be regulated by regulating oligomerization of Fas and FADD.

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